ID A0A177EFG7_9MICR Unreviewed; 1182 AA.
AC A0A177EFG7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094};
GN ORFNames=NEIG_00217 {ECO:0000313|EMBL:OAG30705.1};
OS Nematocida sp. ERTm5.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nematocida.
OX NCBI_TaxID=1805481 {ECO:0000313|EMBL:OAG30705.1, ECO:0000313|Proteomes:UP000077089};
RN [1] {ECO:0000313|EMBL:OAG30705.1, ECO:0000313|Proteomes:UP000077089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERTm5 {ECO:0000313|EMBL:OAG30705.1,
RC ECO:0000313|Proteomes:UP000077089};
RA Reinke A.W., Balla K.M., Bennett E.J., Troemel E.R.;
RT "Identification of microsporidia host-exposed proteins reveals a repertoire
RT of large paralogous families and rapidly evolving proteins.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. {ECO:0000256|RuleBase:RU362094}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAG30705.1}.
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DR EMBL; LTDK01000174; OAG30705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177EFG7; -.
DR VEuPathDB; MicrosporidiaDB:NEIG_00217; -.
DR OrthoDB; 1944951at2759; -.
DR Proteomes; UP000077089; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 424..538
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1088..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 135112 MW; 11466FC04AF537C0 CRC64;
MSQKPKTVEE IYQKKTPIEH VLLRPDTYIG SVQPETRTMY VWCAEKMKMV RKEVTYTPGL
YKIFDEILVN AADNKTRDKR MKEIRIDVDI KNSTISVSND GQGIPVVIHA KENVYVPELI
FGHLLTSSNY DDAEKKMTGG RNGYGAKLCN IFSTKFVIET ADKKNKKKFR QVYTNNMLKK
EEPEIEPFTG EEYTKVTFQP DLAKFSMKRI DDDFMSLIMK RVYDLAGTVG DISVYFNGEK
IPVSNFREYI KLFFDNDVEI VYESKGRWEI AYVLGDEQFQ HVSFVNRIST PRGGTHVNYI
ADQIVSAVVE QAKKVEKGLV VRPIQVKANI FLFLNCLIEN PAFDSQTKET LTLKQSSFGS
KHTLGSKFIS EIMKSGIVEK SAYAARAKQT QQLKKTDGHK TSKLRGIPKL DDANNAGTRY
AAQCTLILTE GDSAKSLAVS GLSVIGRDNY GVFPLRGKLL NVREATHKQL MENMEINNIK
KIMGLQHGKE YATTESLRYG HLMIMTDQDH DGSHIKGLII NMLDHFFPSL LKIKGFLQEF
ITPIVRATKG SMSRDFFTIP EFESWCETSE GRENGWKIKY YKGLGTSTAK DAKDYFSNLD
FHIKEFIPMD STDRDKIELA FSKKRIESRK VWLKEFVPGT YLDNRVQAIS IKNFIDRELI
HFSLADNIRS IPNVIDGMKP GQRKIIYCCF KRQLKSEIKV AQLAGYVSEH SAYHHGEQSL
CSTIVNLAQD YVGSNNIPLL QPIGQFGTRL QGGKDAASPR YIFTALQPIT RYIFREQDDH
LLNYLKDDNL MVEPDMYIPI IPMVLVNGSE GIGTGWSTCI PSYNPIDIVD NVKRMIKGLE
PEDMMPWYKG FAGECEDLGG GKYRTTGTFE LETGKINILE LPIGTWTQNY KDFLETLIES
GDIKDFREYN TDTKVYFEVI VSKQKVNVPK VFKLSSQIST ANMVAFNSKG VLQKYTSPSE
ILKEFYPVRR DLYVRRKDFL LKKLNVEMTI LENKVRFIKE VVADTLKIVK RKSADIVKEL
TEKEYTKKDN SYDYLLTMSI ASLTVERIDK LENESTTKRN EYNTLKNISI EDMWISDLDE
FLKHLDLSVK NDDNPRPKRK GRKIKQPVIS KEIKNQPQKS SKNKKEKVSV LDSDSDFSHT
TVDDSMTSPS HTSKSKGSKP KNSSKSETMP WNRTLLSTDE DD
//
